TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gudelj, Ivan
AU  - Klarić, Thomas
AU  - Hinneburg, Hannes
AU  - Vinković, Marijana
AU  - Wittine, Karlo
AU  - Dovezenski, Nebojša
AU  - Vikić-Topić, Dražen
AU  - Lauc, Gordan
AU  - Vujčić, Zoran
AU  - Josić, Đuro
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3732
AB  - Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stability
is significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionated
by anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability in
regard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.
PB  - Wiley
T2  - Electrophoresis
T1  - Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
VL  - 42
IS  - 24
SP  - 2626
EP  - 2636
DO  - 10.1002/elps.202000092
ER  - 

@article{
author = "Anđelković, Uroš and Gudelj, Ivan and Klarić, Thomas and Hinneburg, Hannes and Vinković, Marijana and Wittine, Karlo and Dovezenski, Nebojša and Vikić-Topić, Dražen and Lauc, Gordan and Vujčić, Zoran and Josić, Đuro",
year = "2021",
abstract = "Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stability
is significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionated
by anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability in
regard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.",
publisher = "Wiley",
journal = "Electrophoresis",
title = "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase",
volume = "42",
number = "24",
pages = "2626-2636",
doi = "10.1002/elps.202000092"
}

Anđelković, U., Gudelj, I., Klarić, T., Hinneburg, H., Vinković, M., Wittine, K., Dovezenski, N., Vikić-Topić, D., Lauc, G., Vujčić, Z.,& Josić, Đ.. (2021). Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis
Wiley., 42(24), 2626-2636.
https://doi.org/10.1002/elps.202000092

Anđelković U, Gudelj I, Klarić T, Hinneburg H, Vinković M, Wittine K, Dovezenski N, Vikić-Topić D, Lauc G, Vujčić Z, Josić Đ. Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis. 2021;42(24):2626-2636.
doi:10.1002/elps.202000092 .

Anđelković, Uroš, Gudelj, Ivan, Klarić, Thomas, Hinneburg, Hannes, Vinković, Marijana, Wittine, Karlo, Dovezenski, Nebojša, Vikić-Topić, Dražen, Lauc, Gordan, Vujčić, Zoran, Josić, Đuro, "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase" in Electrophoresis, 42, no. 24 (2021):2626-2636,
https://doi.org/10.1002/elps.202000092 . .

TY  - JOUR
AU  - Wittine, Karlo
AU  - Antolović, Roberto
AU  - Jelić, Dubravko
AU  - Bracanović, Sara
AU  - Cetina, Mario
AU  - Anđelković, Uroš
AU  - Wittine, Ozren
AU  - Kraljević Pavelić, Sandra
AU  - Vinter, Adrijana
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3614
AB  - Furanocoumarins, particularly furo[3,2-c]coumarins, are found in many natural products. However, coumarins
annulated to a thiophene ring have received scarce attention to date in the literature. Therefore, we synthesized
4-oxo-4H-thieno[3,2-c]chromene derivatives and tested in vitro their anti-inflammatory activity. Anti-inflammatory
potential of the synthesized compounds (1, 2, 6–8, 9a–e and 10a–c) has been evaluated by measuring
various pSTAT (signal transducer and activator of transcription) inhibition within the JAK (Janus-activated
family kinase)/STAT signaling pathway. Ethyl 7-hydroxy-4-oxo-4H-thieno[3,2-c]chromene-2-carboxylate
(7) showed best inhibition properties on pSTAT5 in GM-CSF (Granulocyte-macrophage colony-stimulating
factor)-triggered PBMC assay, with IC50 value of 5.0 μM.
PB  - Elsevier
T2  - Bioorganic & Medicinal Chemistry Letters
T1  - Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines
VL  - 30
IS  - 18
SP  - 127415
DO  - 10.1016/j.bmcl.2020.127415
ER  - 

@article{
author = "Wittine, Karlo and Antolović, Roberto and Jelić, Dubravko and Bracanović, Sara and Cetina, Mario and Anđelković, Uroš and Wittine, Ozren and Kraljević Pavelić, Sandra and Vinter, Adrijana",
year = "2020",
abstract = "Furanocoumarins, particularly furo[3,2-c]coumarins, are found in many natural products. However, coumarins
annulated to a thiophene ring have received scarce attention to date in the literature. Therefore, we synthesized
4-oxo-4H-thieno[3,2-c]chromene derivatives and tested in vitro their anti-inflammatory activity. Anti-inflammatory
potential of the synthesized compounds (1, 2, 6–8, 9a–e and 10a–c) has been evaluated by measuring
various pSTAT (signal transducer and activator of transcription) inhibition within the JAK (Janus-activated
family kinase)/STAT signaling pathway. Ethyl 7-hydroxy-4-oxo-4H-thieno[3,2-c]chromene-2-carboxylate
(7) showed best inhibition properties on pSTAT5 in GM-CSF (Granulocyte-macrophage colony-stimulating
factor)-triggered PBMC assay, with IC50 value of 5.0 μM.",
publisher = "Elsevier",
journal = "Bioorganic & Medicinal Chemistry Letters",
title = "Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines",
volume = "30",
number = "18",
pages = "127415",
doi = "10.1016/j.bmcl.2020.127415"
}

Wittine, K., Antolović, R., Jelić, D., Bracanović, S., Cetina, M., Anđelković, U., Wittine, O., Kraljević Pavelić, S.,& Vinter, A.. (2020). Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines. in Bioorganic & Medicinal Chemistry Letters
Elsevier., 30(18), 127415.
https://doi.org/10.1016/j.bmcl.2020.127415

Wittine K, Antolović R, Jelić D, Bracanović S, Cetina M, Anđelković U, Wittine O, Kraljević Pavelić S, Vinter A. Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines. in Bioorganic & Medicinal Chemistry Letters. 2020;30(18):127415.
doi:10.1016/j.bmcl.2020.127415 .

Wittine, Karlo, Antolović, Roberto, Jelić, Dubravko, Bracanović, Sara, Cetina, Mario, Anđelković, Uroš, Wittine, Ozren, Kraljević Pavelić, Sandra, Vinter, Adrijana, "Thienochromene derivatives inhibit pSTAT1 and pSTAT5 signaling induced by cytokines" in Bioorganic & Medicinal Chemistry Letters, 30, no. 18 (2020):127415,
https://doi.org/10.1016/j.bmcl.2020.127415 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Gudelj, Ivan
AU  - Klarić, Thomas
AU  - Hinneburg, Hannes
AU  - Vinković, Marijana
AU  - Wittine, Karlo
AU  - Dovezenski, Nebojša
AU  - Vikić-Topić, Dražen
AU  - Lauc, Gordan
AU  - Vujčić, Zoran
AU  - Josić, Đuro
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3989
AB  - Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.
PB  - Wiley
T2  - Electrophoresis
T1  - Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
DO  - 10.1002/elps.202000092
ER  - 

@article{
author = "Anđelković, Uroš and Gudelj, Ivan and Klarić, Thomas and Hinneburg, Hannes and Vinković, Marijana and Wittine, Karlo and Dovezenski, Nebojša and Vikić-Topić, Dražen and Lauc, Gordan and Vujčić, Zoran and Josić, Đuro",
year = "2020",
abstract = "Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports.",
publisher = "Wiley",
journal = "Electrophoresis",
title = "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase",
doi = "10.1002/elps.202000092"
}

Anđelković, U., Gudelj, I., Klarić, T., Hinneburg, H., Vinković, M., Wittine, K., Dovezenski, N., Vikić-Topić, D., Lauc, G., Vujčić, Z.,& Josić, Đ.. (2020). Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis
Wiley..
https://doi.org/10.1002/elps.202000092

Anđelković U, Gudelj I, Klarić T, Hinneburg H, Vinković M, Wittine K, Dovezenski N, Vikić-Topić D, Lauc G, Vujčić Z, Josić Đ. Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase. in Electrophoresis. 2020;.
doi:10.1002/elps.202000092 .

Anđelković, Uroš, Gudelj, Ivan, Klarić, Thomas, Hinneburg, Hannes, Vinković, Marijana, Wittine, Karlo, Dovezenski, Nebojša, Vikić-Topić, Dražen, Lauc, Gordan, Vujčić, Zoran, Josić, Đuro, "Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase" in Electrophoresis (2020),
https://doi.org/10.1002/elps.202000092 . .

TY  - JOUR
AU  - Malatesti, Nela
AU  - Harej, Anja
AU  - Kraljević Pavelić, Sandra
AU  - Lončarić, M.
AU  - Zorc, H.
AU  - Wittine, Karlo
AU  - Anđelković, Uroš
AU  - Josić, Djuro
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6916
AB  - Photodynamic therapy (PDT) is a treatment that aims to kill cancer cells by reactive oxygen species, mainly singlet oxygen, produced through light activation of a photosensitiser (PS). Amongst photosensitisers that attracted the most attention in the last decade are cationic and amphiphilic molecules based on porphyrin, chlorin and phthalocyanine structures. Our aim was to join this search for more optimal balance of the lipophilic and hydrophilic moieties in a PS. A new amphiphilic porphyrin, 5-(4-octadecanamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride (5) was synthesised and characterised by 1H NMR, UV–vis and fluorescence spectroscopy, and by MALDI-TOF/TOF spectrometry. In vitro photodynamic activity of 5 was evaluated on HeLa cell lines and compared to the activity of the hydrophilic 5-(4-acetamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride (7). Low fluence rate (2 mW cm−2) of red light (643 nm) was used for the activation, and both porphyrins showed a drug dose-response as well as a light dose-response relationship, but the amphiphilic porphyrin was presented with significantly lower IC50 values. The obtained IC50 values for 5 were 1.4 μM at 15 min irradiation time and 0.7 μM when the time of irradiation was 30 min, while for 7 these values were 37 and 6 times higher, respectively. These results confirm the importance of the lipophilic component in a PS and show a potential for 5 to be used as a PS in PDT applications.
PB  - Elsevier
T2  - Photodiagnosis and Photodynamic Therapy
T1  - Synthesis, characterisation and in vitro investigation of photodynamic activity of 5-(4-octadecanamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride on HeLa cells using low light fluence rate
VL  - 15
SP  - 115
EP  - 126
DO  - 10.1016/j.pdpdt.2016.07.003
ER  - 

@article{
author = "Malatesti, Nela and Harej, Anja and Kraljević Pavelić, Sandra and Lončarić, M. and Zorc, H. and Wittine, Karlo and Anđelković, Uroš and Josić, Djuro",
year = "2016",
abstract = "Photodynamic therapy (PDT) is a treatment that aims to kill cancer cells by reactive oxygen species, mainly singlet oxygen, produced through light activation of a photosensitiser (PS). Amongst photosensitisers that attracted the most attention in the last decade are cationic and amphiphilic molecules based on porphyrin, chlorin and phthalocyanine structures. Our aim was to join this search for more optimal balance of the lipophilic and hydrophilic moieties in a PS. A new amphiphilic porphyrin, 5-(4-octadecanamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride (5) was synthesised and characterised by 1H NMR, UV–vis and fluorescence spectroscopy, and by MALDI-TOF/TOF spectrometry. In vitro photodynamic activity of 5 was evaluated on HeLa cell lines and compared to the activity of the hydrophilic 5-(4-acetamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride (7). Low fluence rate (2 mW cm−2) of red light (643 nm) was used for the activation, and both porphyrins showed a drug dose-response as well as a light dose-response relationship, but the amphiphilic porphyrin was presented with significantly lower IC50 values. The obtained IC50 values for 5 were 1.4 μM at 15 min irradiation time and 0.7 μM when the time of irradiation was 30 min, while for 7 these values were 37 and 6 times higher, respectively. These results confirm the importance of the lipophilic component in a PS and show a potential for 5 to be used as a PS in PDT applications.",
publisher = "Elsevier",
journal = "Photodiagnosis and Photodynamic Therapy",
title = "Synthesis, characterisation and in vitro investigation of photodynamic activity of 5-(4-octadecanamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride on HeLa cells using low light fluence rate",
volume = "15",
pages = "115-126",
doi = "10.1016/j.pdpdt.2016.07.003"
}

Malatesti, N., Harej, A., Kraljević Pavelić, S., Lončarić, M., Zorc, H., Wittine, K., Anđelković, U.,& Josić, D.. (2016). Synthesis, characterisation and in vitro investigation of photodynamic activity of 5-(4-octadecanamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride on HeLa cells using low light fluence rate. in Photodiagnosis and Photodynamic Therapy
Elsevier., 15, 115-126.
https://doi.org/10.1016/j.pdpdt.2016.07.003

Malatesti N, Harej A, Kraljević Pavelić S, Lončarić M, Zorc H, Wittine K, Anđelković U, Josić D. Synthesis, characterisation and in vitro investigation of photodynamic activity of 5-(4-octadecanamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride on HeLa cells using low light fluence rate. in Photodiagnosis and Photodynamic Therapy. 2016;15:115-126.
doi:10.1016/j.pdpdt.2016.07.003 .

Malatesti, Nela, Harej, Anja, Kraljević Pavelić, Sandra, Lončarić, M., Zorc, H., Wittine, Karlo, Anđelković, Uroš, Josić, Djuro, "Synthesis, characterisation and in vitro investigation of photodynamic activity of 5-(4-octadecanamidophenyl)-10,15,20-tris(N-methylpyridinium-3-yl)porphyrin trichloride on HeLa cells using low light fluence rate" in Photodiagnosis and Photodynamic Therapy, 15 (2016):115-126,
https://doi.org/10.1016/j.pdpdt.2016.07.003 . .